Three Dimensional Structure of Human Fibrinogen under Aqueous Conditions Visualized by Atomic Force Microscopy

Roger E Marchant; Matthew D Barb; John R Shainoff; Steven J Eppell; David L Wilson; Christopher A Siedlecki

doi:10.1055/s-0038-1656109

Thrombosis and Haemostasis, Table of Contents

Thromb Haemost 1997; 77(06): 1048-1051
DOI: 10.1055/s-0038-1656109

Rapid Communications

Schattauer GmbH Stuttgart

Three Dimensional Structure of Human Fibrinogen under Aqueous Conditions Visualized by Atomic Force Microscopy

Authors

Roger E Marchant

¹The Department of Biomedical Engineering, Cleveland Clinic Foundation, Cleveland, Ohio, USA

²Department of Macromolecular Science, Case Western Reserve University, Cleveland Clinic Foundation, Cleveland, Ohio, USA
Matthew D Barb

¹The Department of Biomedical Engineering, Cleveland Clinic Foundation, Cleveland, Ohio, USA
John R Shainoff

³The Department of Cell Biology, Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio, USA
Steven J Eppell

¹The Department of Biomedical Engineering, Cleveland Clinic Foundation, Cleveland, Ohio, USA
David L Wilson

¹The Department of Biomedical Engineering, Cleveland Clinic Foundation, Cleveland, Ohio, USA
Christopher A Siedlecki

¹The Department of Biomedical Engineering, Cleveland Clinic Foundation, Cleveland, Ohio, USA

Abstract

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Summary

Fibrinogen plays a central role in surface-induced thrombosis. However, the interactions of fibrinogen with different substrata remain poorly understood because of the difficulties involved in imaging globular proteins under aqueous conditions. We present detailed three dimensional molecular scale images of fibrinogen molecules on a hydrophobic surface under aqueous conditions obtained by atomic force microscopy. Hydrated fibrinogen monomers are visualized as overlapping ellipsoids; dimers and trimers have linear conformations predominantly, and increased affinity for the hydrophobic surface compared with monomeric fibrinogen. The results demonstrate the importance of hydration on protein structure and properties that affect surface-dependent interactions.

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References

References
1 Hantgan RR, Francis CW, Marder VJ. Fibrinogen structure and physiology. In: Hemostasis and Thrombosis: Basic Principles and Clinical Practice. Colman RW, Hirsh J, Marder VJ, Salzman EW. (eds) 03. edition J. B. Lippincott Company; Philadelphia, PA: 1994. pp 277-300
2 Davies MJ. A macroscopic and microscopic view of coronary thrombosis. Circulation 1990; 82 (Suppl. 02) 38-44
3 Lassila R, Peltonen S, Lepantalo M, Saarinen O, Kauhanen P, Manninen V. Severity of peripheral atherosclerosis is associated with fibrinogen and degradation of crosslinked fibrin. Atherioscler Thromb 1993; 13: 1738-1742
4 Bini A, Fenoglio JJ, Mesa-Tejada R, Kudryk B, Kaplan KL. Identification and distribution of fibrinogen, fibrin, and fibrin(ogen) degradation products in atherosclerosis. Use of monoclonal antibodies. Arteriosclerosis 1989; 09: 109-121
5 Valenzuela RJ, Shainoff R, Dibello PM, Urbanic DA, Anderson JM, Matsueda GR, Kudryk BJ. Immunoelectrophoretic and immunohistochemical characterization of fibrinogen derivatives in atherosclerotic aortic intimas and vascular prosthesis pseudo-intimas. Am J Pathol 1992; 141: 861-880
6 Hanson SR. Device Thrombosis and thromboembolism. Cardiovasc Pathol 1993; 02: 157S-165S
7 Hall CE, Slayter HS. The fibrinogen molecule: Its size, shape, and mode of polymerization. J Biophys Biochem Cytol 1959; 05: 11-16
8 Fowler WE, Erickson HP. Trinodular Structure of fibrinogen, Confirmation by both shadowing and negative stain microscopy. J Mol Biol 1979; 134: 241-249
9 Weisel JW, Philips Jr GN, Cohen C. A model from electron microscopy for the molecular structure of fibrinogen and fibrin. Nature 1981; 289: 263-267
10 Cohen C, Weisel JW, Phillips Jr GN, Stauffacher CV, Fillers JP, Daub E. The structure of fibrinogen and fibrin: I Electron microscopy and X-ray crystallography of fibrinogen. In: Molecular Biology of Fibrinogen and Fibrin. Mosesson MW, Doolittle RF. eds Ann NY Acad Sci, NY; 1983. 408. 194-213
11 Weisel JW, Stauffacher CV, Bullitt E, Cohen C. A model for Fibrinogen. Science 1985; 230: 1388-1391
12 Drake B, Prater CB, Weisenhorn AL, Gould SA, Albrecht TR, Quate CF, Cannell DS, Hansma HG, Hansma PK. Imaging crystals, polymers, and processes in water with the atomic force microscope. Science 1989; 243: 1586-1589
13 Marchant RE, Lea S, Andrade JD, Bockenstedt P. Interactions of von Willebrand factor on mica studied by atomic force microscopy. J Colloid & Interface Sci 1992; 148: 261-271
14 Shainoff JR, Urbanic DA, DiBello PM. Immunoelectrophoretic characterizations of the cross-linking of fibrinogen and fibrin by plasma and tissue-transglutaminase. Identification of a rapid mode of hybrid α/γ-chain crosslinking that is promoted by the 7-chain cross-linking. J Biol Chem 1991; 266: 6429-6437
15 Keller DJ, Chih-Chung C. Imaging steep high structures by scanning force microscopy with electron beam deposited tips. Surface Sci 1992; 268: 333-339
16 Eppell SJ, Simmons RS, Albrecht RM, Marchant RE. Cell-surface receptors and proteins on platelet membranes imaged by scanning force microscopy using immunogold contrast enhancement. Biophys J 1995; 68: 671-680
17 Siedlecki CA, Eppell SJ, Marchant RE. Interactions of human von Willebrand factor with a hydrophobic self-assembled monolayer studied by atomic force microscopy. J Biomed Mater Res 1994; 28: 971-980
18 Fowler WE, Erickson HP, Hantgan RR, Mc DonaghJ, Hermans J. Crosslinked fibrinogen dimers demonstrate a feature of the molecular packing in fibrin fibers. Science 1981; 211: 287-289
19 Weisel JW, Francis CW, Chandrasekaran N, Marder VJ. Examination of the platelet membrane glycoprotein Ilb-IIIa complex and its interactions with fibrinogen and other ligands by electron microscopy. J Biol Chem 1992; 267: 16637-16643
20 Mosesson MW, Siebenlist KR, Hainfeld JF, Wall JS. The covalent structure of Factor XIIIa crosslinked fibrinogen fibrils. J Struc Biol 1995; 115: 88-101
21 Siedlecki CA, Lestini B, Kottke-Marchant K, Eppell S, Wilson D, Marchant RE. Shear dependent changes in the three dimensional structure of human von Willebrand factor. Blood 1996; 88: 2939-2950
22 Wilson DL, Dalai P, Kump KS, Benard W, Ping X, Marchant RE, Eppell SJ. Morphological modeling of AFM imaging including nanostructure probes and fibrinogen molecules. J Vac Sci & Technol B 1996; 14: 2407-2416